ID   OXLA_BOTMA              Reviewed;          39 AA.
AC   P0CJ40;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 1.
DT   25-MAY-2022, entry version 24.
DE   RecName: Full=L-amino-acid oxidase;
DE            Short=BmarLAAO {ECO:0000303|PubMed:19944711};
DE            Short=LAO;
DE            EC=1.4.3.2 {ECO:0000269|PubMed:19944711};
DE   Flags: Fragment;
OS   Bothrops marajoensis (Marajo lancehead).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Viperidae; Crotalinae; Bothrops.
OX   NCBI_TaxID=157554;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND CATALYTIC
RP   ACTIVITY.
RC   TISSUE=Venom;
RX   PubMed=19944711; DOI=10.1016/j.toxicon.2009.11.013;
RA   Costa Torres A.F., Dantas R.T., Toyama M.H., Diz Filho E.B., Zara F.J.,
RA   Rodrigues de Queiroz M.G., Pinto Nogueira N.A., Rosa de Oliveira M.,
RA   de Oliveira Toyama D., Monteiro H.S.A., Martins A.M.C.;
RT   "Antibacterial and antiparasitic effects of Bothrops marajoensis venom and
RT   its fractions: phospholipase A2 and L-amino acid oxidase.";
RL   Toxicon 55:795-804(2010).
CC   -!- FUNCTION: Catalyzes an oxidative deamination of predominantly
CC       hydrophobic and aromatic L-amino acids, thus producing hydrogen
CC       peroxide that may contribute to the diverse toxic effects of this
CC       enzyme (PubMed:19944711). Shows activity on L-Leu (PubMed:19944711).
CC       Exhibits diverse biological activities, such as hemorrhage, hemolysis,
CC       edema, apoptosis of vascular endothelial cells or tumor cell lines, and
CC       antiparasitic activities, as well as regulation of platelet
CC       aggregation. Effects of snake L-amino oxidases on platelets are
CC       controversial, since they either induce aggregation or inhibit agonist-
CC       induced aggregation. These different effects are probably due to
CC       different experimental conditions (By similarity). In addition, this
CC       protein inhibits dose-dependently the growth of Gram-positive, Gram-
CC       negative bacteria and yeast, probably by the generation of hydrogen
CC       peroxide. {ECO:0000250|UniProtKB:P0CC17, ECO:0000269|PubMed:19944711}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an L-alpha-amino acid + H2O + O2 = a 2-oxocarboxylate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:13781, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:28938, ChEBI:CHEBI:35179,
CC         ChEBI:CHEBI:59869; EC=1.4.3.2;
CC         Evidence={ECO:0000269|PubMed:19944711};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-leucine + O2 = 4-methyl-2-oxopentanoate + H2O2 +
CC         NH4(+); Xref=Rhea:RHEA:60996, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379,
CC         ChEBI:CHEBI:16240, ChEBI:CHEBI:17865, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:57427; Evidence={ECO:0000269|PubMed:19944711};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000250|UniProtKB:P81382};
CC   -!- SUBUNIT: Monomer. This is in contrast with most of its orthologs, that
CC       are non-covalently linked homodimers. {ECO:0000269|PubMed:19944711}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19944711}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000305|PubMed:19944711}.
CC   -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:P81382}.
CC   -!- MISCELLANEOUS: Has parasiticidal activities against leishmania, as a
CC       result of enzyme-catalyzed hydrogen peroxide production.
CC       {ECO:0000305|PubMed:19944711}.
CC   -!- SIMILARITY: Belongs to the flavin monoamine oxidase family. FIG1
CC       subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P0CJ40; -.
DR   SMR; P0CJ40; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0001716; F:L-amino-acid oxidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0042742; P:defense response to bacterium; IEA:UniProtKB-KW.
DR   GO; GO:0050832; P:defense response to fungus; IEA:UniProtKB-KW.
DR   GO; GO:0044179; P:hemolysis in another organism; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Antibiotic; Antimicrobial; Apoptosis; Cytolysis; Direct protein sequencing;
KW   Disulfide bond; FAD; Flavoprotein; Fungicide; Glycoprotein; Hemolysis;
KW   Hemostasis impairing toxin; Oxidoreductase; Secreted; Toxin.
FT   CHAIN           1..>39
FT                   /note="L-amino-acid oxidase"
FT                   /id="PRO_0000412597"
FT   DISULFID        10..?
FT                   /evidence="ECO:0000250|UniProtKB:P81382"
FT   NON_TER         39
FT                   /evidence="ECO:0000303|PubMed:19944711"
SQ   SEQUENCE   39 AA;  4405 MW;  5A9BBD388988C742 CRC64;
     AHDGNPLEEC FREDDEEFFL EIAKNGLTAT SNPKRVVIV